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Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Factor A) (FA) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)

 GSK3B_RAT               Reviewed;         420 AA.
P18266;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 182.
RecName: Full=Glycogen synthase kinase-3 beta;
Short=GSK-3 beta;
EC=2.7.11.26;
AltName: Full=Factor A;
Short=FA;
AltName: Full=Serine/threonine-protein kinase GSK3B;
EC=2.7.11.1;
Name=Gsk3b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=2164470;
Woodgett J.R.;
"Molecular cloning and expression of glycogen synthase kinase-3/factor
A.";
EMBO J. 9:2431-2438(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
PubMed=7686508; DOI=10.1016/0014-5793(93)81066-9;
Ishiguro K., Shiratsuchi A., Sato S., Omori A., Arioka M.,
Kobayashi S., Uchida T., Imahori K.;
"Glycogen synthase kinase 3 beta is identical to tau protein kinase I
generating several epitopes of paired helical filaments.";
FEBS Lett. 325:167-172(1993).
[3]
PHOSPHORYLATION AT TYR-216, AND MUTAGENESIS OF TYR-216.
PubMed=8382613;
Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.;
"Modulation of the glycogen synthase kinase-3 family by tyrosine
phosphorylation.";
EMBO J. 12:803-808(1993).
[4]
FUNCTION, AND INTERACTION WITH CTNNB1/BETA-CATENIN.
PubMed=9482734; DOI=10.1093/emboj/17.5.1371;
Ikeda S., Kishida S., Yamamoto H., Murai H., Koyama S., Kikuchi A.;
"Axin, a negative regulator of the Wnt signaling pathway, forms a
complex with GSK-3beta and beta-catenin and promotes GSK-3beta-
dependent phosphorylation of beta-catenin.";
EMBO J. 17:1371-1384(1998).
[5]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MACF1; APC;
AXIN1 AND CTNNB1.
PubMed=16815997; DOI=10.1101/gad.1411206;
Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
"The role of microtubule actin cross-linking factor 1 (MACF1) in the
Wnt signaling pathway.";
Genes Dev. 20:1933-1945(2006).
[6]
FUNCTION IN REGULATION OF PANCREATIC BETA-CELLS.
PubMed=17242403; DOI=10.1074/jbc.M609637200;
Mussmann R., Geese M., Harder F., Kegel S., Andag U., Lomow A.,
Burk U., Onichtchouk D., Dohrmann C., Austen M.;
"Inhibition of GSK3 promotes replication and survival of pancreatic
beta cells.";
J. Biol. Chem. 282:12030-12037(2007).
[7]
FUNCTION IN PHOSPHORYLATION OF MARK2, AND MUTAGENESIS OF SER-9.
PubMed=18424437; DOI=10.1074/jbc.M706596200;
Timm T., Balusamy K., Li X., Biernat J., Mandelkow E., Mandelkow E.M.;
"Glycogen synthase kinase (GSK) 3beta directly phosphorylates Serine
212 in the regulatory loop and inhibits microtubule affinity-
regulating kinase (MARK) 2.";
J. Biol. Chem. 283:18873-18882(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Constitutively active protein kinase that acts as a
negative regulator in the hormonal control of glucose homeostasis,
Wnt signaling and regulation of transcription factors and
microtubules, by phosphorylating and inactivating glycogen
synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1,
DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires
primed phosphorylation of the majority of its substrates. In
skeletal muscle, contributes to insulin regulation of glycogen
synthesis by phosphorylating and inhibiting GYS1 activity and
hence glycogen synthesis. May also mediate the development of
insulin resistance by regulating activation of transcription
factors. Regulates protein synthesis by controlling the activity
of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as
glycogen synthase. In Wnt signaling, GSK3B forms a multimeric
complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates
the N-terminus of CTNNB1 leading to its degradation mediated by
ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its
DNA-binding domain, thereby reducing its affinity for DNA.
Phosphorylates NFATC1/NFATC on conserved serine residues promoting
NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene
regulation, and thereby opposing the action of calcineurin.
Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly
MAPT/TAU ability to bind and stabilize microtubules. Plays an
important role in ERBB2-dependent stabilization of microtubules at
the cell cortex. Phosphorylates MACF1, inhibiting its binding to
microtubules which is critical for its role in bulge stem cell
migration and skin wound repair. Probably regulates NF-kappa-B
(NFKB1) at the transcriptional level and is required for the NF-
kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA).
Negatively regulates replication in pancreatic beta-cells,
resulting in apoptosis, loss of beta-cells. Through
phosphorylation of the anti-apoptotic protein MCL1, may control
cell apoptosis in response to growth factors deprivation.
Phosphorylates MUC1 in breast cancer cells, decreasing the
interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the
establishment of neuronal polarity and axon outgrowth.
Phosphorylates MARK2, leading to inhibit its activity.
Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity.
Phosphorylates ZC3HAV1 which enhances its antiviral activity.
Phosphorylates SFPQ upon T-cell activation. Phosphorylates SNAI1,
leading to its BTRC-triggered ubiquitination and proteasomal
degradation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and
stabilizes it by protecting it from proteasomal degradation.
Regulates the circadian clock via phosphorylation of the major
clock components including ARNTL/BMAL1, CLOCK and PER2.
Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal
degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21'
and primes it for ubiquitination and proteasomal degradation.
Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively
regulates its activity. {ECO:0000269|PubMed:17242403,
ECO:0000269|PubMed:18424437, ECO:0000269|PubMed:9482734}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation at Tyr-216. In
response to insulin, inhibited by phosphorylation at Ser-9 by
PKB/AKT1; phosphorylation at this site causes a conformational
change, preventing access of substrates to the active site.
Inhibited by lithium.
-!- SUBUNIT: Monomer. Interacts with DAB2IP (via C2 domain); the
interaction stimulates GSK3B kinase activation. Interacts (via C2
domain) with PPP2CA (By similarity). Interacts with ARRB2, AXIN1,
CABYR, DISC1, MMP2, MUC1, NIN, PRUNE1 and ZBED3 (By similarity).
Interacts with AXIN1; the interaction mediates
hyperphosphorylation of CTNNB1 leading to its ubiquitination and
destruction. Interacts with and phosphorylates SNAI1. Interacts
with DNM1L (via a C-terminal domain) (By similarity). Found in a
complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts
with SGK3. Interacts with the CLOCK-ARNTL/BMAL1 heterodimer.
Interacts with the ARNTL/BMAL1 (By similarity). Interacts with
CTNND2 (By similarity). The complex composed, at least, of APC,
CTNNB1 and GSK3B interacts with JPT1; the interaction requires the
inactive form of GSK3B (phosphorylated at 'Ser-9') (By
similarity). Forms a complex composed of PRKAR2A or PRKAR2B, GSK3B
and GSKIP through GSKIP interaction; facilitates PKA-induced
phosphorylation and regulates GSK3B activity. Interacts with
GSK3B; induces GSK3B-mediated phosphorylation of GSKIP (By
similarity). {ECO:0000250|UniProtKB:P49841,
ECO:0000250|UniProtKB:Q9WV60}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Membrane {ECO:0000269|PubMed:16815997}. Cell
membrane {ECO:0000250}. Note=The phosphorylated form shows
localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1
signaling pathway controls localization of the phosphorylated form
to the cell membrane (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated
signaling, the activated PKB/AKT1 and RPS6KA3 protein kinases
phosphorylate and desactivate GSK3B, resulting in the
dephosphorylation and activation of GYS1. Activated by
phosphorylation at Tyr-216 (By similarity). Inactivated by
phosphorylation at Ser-9 (By similarity).
{ECO:0000250|UniProtKB:P49841, ECO:0000250|UniProtKB:Q9WV60}.
-!- PTM: Mono-ADP-ribosylation by PARP10 negatively regulates kinase
activity. {ECO:0000250}.
-!- MISCELLANEOUS: Simultaneous silencing of GSK3A and GSK3B by RNAi
stimulates replication and promotes survival of INS-1E pancreatic
beta cells. {ECO:0000305|PubMed:17242403}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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EMBL; X53428; CAA37519.1; -; mRNA.
EMBL; X73653; CAA52020.1; -; mRNA.
PIR; S14708; TVRTKB.
RefSeq; NP_114469.1; NM_032080.1.
UniGene; Rn.10426; -.
ProteinModelPortal; P18266; -.
SMR; P18266; -.
BioGrid; 249893; 9.
CORUM; P18266; -.
DIP; DIP-40957N; -.
IntAct; P18266; 1.
MINT; MINT-121872; -.
STRING; 10116.ENSRNOP00000003867; -.
BindingDB; P18266; -.
ChEMBL; CHEMBL3669; -.
iPTMnet; P18266; -.
PhosphoSitePlus; P18266; -.
PaxDb; P18266; -.
PRIDE; P18266; -.
GeneID; 84027; -.
KEGG; rno:84027; -.
UCSC; RGD:70982; rat.
CTD; 2932; -.
RGD; 70982; Gsk3b.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233017; -.
HOVERGEN; HBG014652; -.
InParanoid; P18266; -.
KO; K03083; -.
PhylomeDB; P18266; -.
TreeFam; TF101104; -.
BRENDA; 2.7.11.26; 5301.
PRO; PR:P18266; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:BHF-UCL.
GO; GO:0044297; C:cell body; ISO:RGD.
GO; GO:0005813; C:centrosome; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0030426; C:growth cone; ISO:RGD.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043227; C:membrane-bounded organelle; ISO:RGD.
GO; GO:0005874; C:microtubule; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; ISO:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:1990909; C:Wnt signalosome; ISO:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
GO; GO:0070840; F:dynein complex binding; ISO:RGD.
GO; GO:0005178; F:integrin binding; IPI:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0016301; F:kinase activity; IDA:RGD.
GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
GO; GO:0002039; F:p53 binding; ISO:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:RGD.
GO; GO:0048156; F:tau protein binding; IDA:RGD.
GO; GO:0050321; F:tau-protein kinase activity; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0007409; P:axonogenesis; ISO:RGD.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; ISO:RGD.
GO; GO:0016477; P:cell migration; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
GO; GO:1903351; P:cellular response to dopamine; IEP:RGD.
GO; GO:0036018; P:cellular response to erythropoietin; IEP:RGD.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0036016; P:cellular response to interleukin-3; ISS:UniProtKB.
GO; GO:0071282; P:cellular response to iron(II) ion; IEP:RGD.
GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0006983; P:ER overload response; ISO:RGD.
GO; GO:0030010; P:establishment of cell polarity; IDA:RGD.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:RGD.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
GO; GO:0021766; P:hippocampus development; ISO:RGD.
GO; GO:0044027; P:hypermethylation of CpG island; ISO:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
GO; GO:0007520; P:myoblast fusion; ISO:RGD.
GO; GO:0014902; P:myotube differentiation; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
GO; GO:2000171; P:negative regulation of dendrite development; IMP:RGD.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:1904339; P:negative regulation of dopaminergic neuron differentiation; IMP:RGD.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
GO; GO:0014043; P:negative regulation of neuron maturation; ISO:RGD.
GO; GO:2001223; P:negative regulation of neuron migration; IMP:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
GO; GO:0051534; P:negative regulation of NFAT protein import into nucleus; ISS:UniProtKB.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:RGD.
GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
GO; GO:0031333; P:negative regulation of protein complex assembly; ISO:RGD.
GO; GO:1904780; P:negative regulation of protein localization to centrosome; ISO:RGD.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:BHF-UCL.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IMP:RGD.
GO; GO:0032007; P:negative regulation of TOR signaling; ISO:RGD.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
GO; GO:0016310; P:phosphorylation; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:RGD.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0010822; P:positive regulation of mitochondrion organization; ISO:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:RGD.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISO:RGD.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:2000738; P:positive regulation of stem cell differentiation; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
GO; GO:0006611; P:protein export from nucleus; ISO:RGD.
GO; GO:0035372; P:protein localization to microtubule; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0000320; P:re-entry into mitotic cell cycle; ISO:RGD.
GO; GO:0030516; P:regulation of axon extension; IMP:RGD.
GO; GO:0050770; P:regulation of axonogenesis; IMP:RGD.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; ISO:RGD.
GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:1990776; P:response to angiotensin; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0071871; P:response to epinephrine; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:1990418; P:response to insulin-like growth factor stimulus; IEP:RGD.
GO; GO:1902065; P:response to L-glutamate; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:1990478; P:response to ultrasound; IEP:RGD.
GO; GO:0071109; P:superior temporal gyrus development; ISO:RGD.
GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
InterPro; IPR033573; GSK3B.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24057:SF8; PTHR24057:SF8; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ADP-ribosylation; ATP-binding; Biological rhythms;
Carbohydrate metabolism; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Glycogen metabolism; Kinase;
Membrane; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase;
Signal transduction inhibitor; Transferase; Wnt signaling pathway.
CHAIN 1 420 Glycogen synthase kinase-3 beta.
/FTId=PRO_0000085982.
DOMAIN 56 340 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 62 70 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 181 181 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 85 85 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 9 9 Phosphoserine; by PKB/AKT1, RPS6KA3 and
SGK3. {ECO:0000250|UniProtKB:P49841}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000269|PubMed:8382613}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 9 9 S->A: Loss of phosphorylation; No
inhibition of activity.
{ECO:0000269|PubMed:18424437}.
MUTAGEN 216 216 Y->F: Loss of phosphorylation and strong
reduction of activity.
{ECO:0000269|PubMed:8382613}.
CONFLICT 240 240 M -> V (in Ref. 2; CAA52020).
{ECO:0000305}.
SEQUENCE 420 AA; 46742 MW; 2F473FCAB89B4398 CRC64;
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK
VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR
DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDM
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF
NFTTQELSSN PPLATILIPP HARIQAAASP PANATAASDT NAGDRGQTNN AASASASNST


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E2298r ELISA FA,Factor A,Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase GSK3B 96T
U2298r CLIA kit FA,Factor A,Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase GSK3B 96T
E2298r ELISA kit FA,Factor A,Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase GSK3B 96T
U2298r CLIA FA,Factor A,Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase GSK3B 96T
E2298r FA,Factor A,Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase GSK3B
U2298h CLIA kit Glycogen synthase kinase-3 beta,GSK-3 beta,GSK3B,Homo sapiens,Human,Serine_threonine-protein kinase GSK3B 96T
E2298h ELISA Glycogen synthase kinase-3 beta,GSK-3 beta,GSK3B,Homo sapiens,Human,Serine_threonine-protein kinase GSK3B 96T
U2298h CLIA Glycogen synthase kinase-3 beta,GSK-3 beta,GSK3B,Homo sapiens,Human,Serine_threonine-protein kinase GSK3B 96T
E2298h ELISA kit Glycogen synthase kinase-3 beta,GSK-3 beta,GSK3B,Homo sapiens,Human,Serine_threonine-protein kinase GSK3B 96T
E2298m ELISA Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Mouse,Mus musculus,Serine_threonine-protein kinase GSK3B 96T
E2298h Glycogen synthase kinase-3 beta,GSK-3 beta,GSK3B,Homo sapiens,Human,Serine_threonine-protein kinase GSK3B
E2298m ELISA kit Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Mouse,Mus musculus,Serine_threonine-protein kinase GSK3B 96T
U2298m CLIA Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Mouse,Mus musculus,Serine_threonine-protein kinase GSK3B 96T
U2298m CLIA kit Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Mouse,Mus musculus,Serine_threonine-protein kinase GSK3B 96T
E2298m Glycogen synthase kinase-3 beta,GSK-3 beta,Gsk3b,Mouse,Mus musculus,Serine_threonine-protein kinase GSK3B
DL-GSK3b-Hu Human Glycogen Synthase Kinase 3 Beta (GSK3b) ELISA Kit 96T
DL-GSK3b-Ra Rat Glycogen Synthase Kinase 3 Beta (GSK3b) ELISA Kit 96T
SPC-169C GSK-3Beta Antibody, Glycogen Synthase kinase 3 beta, GSK 3 beta, GSK 3B, GSK-3 beta, GSK3B, GSK3B_Human, GSK3beta isoform, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 25ug
SPC-169D GSK-3Beta Antibody, Glycogen Synthase kinase 3 beta, GSK 3 beta, GSK 3B, GSK-3 beta, GSK3B, GSK3B_Human, GSK3beta isoform, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 100ug
GSK3B-1022H Protein Recombinant Human Glycogen Synthase Kinase 3 Beta, His-tagged 5
GSK3B-1022H Protein: Recombinant Human Glycogen Synthase Kinase 3 Beta, His-tagged 5
AP06391PU-N Glycogen Synthase Kinase 3 beta (GSK3b) 100 µg
AM09012PU-N Glycogen Synthase Kinase 3 beta (GSK3b) 0.1 ml
MC829 Glycogen Synthase Kinase 3 beta (GSK3b) 0.1 mg
AM09012PU-S Glycogen Synthase Kinase 3 beta (GSK3b) 50 µl


 

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